| Code | CSB-RA821323A0HU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
| IF | 1:50-1:200 |
| FC | 1:50-1:200 |
Cold-inducible RNA-binding protein (CIRBP) serves as a critical stress-response mediator that becomes upregulated under conditions of mild hypothermia, hypoxia, and UV irradiation. This glycine-rich RNA-binding protein stabilizes specific mRNA transcripts and modulates their translation, influencing cellular processes ranging from circadian rhythm regulation to inflammatory responses. CIRBP has garnered significant research attention for its emerging roles in cancer biology, where it can promote tumor cell survival and proliferation, as well as in inflammatory conditions where extracellular CIRBP acts as a damage-associated molecular pattern.
This recombinant monoclonal antibody, clone 11A9, offers the reproducibility and consistency that demanding research applications require. Generated against a synthetic peptide derived from human CIRBP, the antibody is produced using recombinant technology, ensuring sequence-defined specificity and eliminating the lot-to-lot variability that can compromise longitudinal studies. Affinity chromatography purification delivers a reagent optimized for reliable performance across experiments.
Validation studies demonstrate robust performance across multiple platforms. Immunohistochemistry on paraffin-embedded human tissues reveals clear CIRBP detection in both breast cancer and stomach tissue sections at 1:100 dilution using citrate buffer antigen retrieval. Immunofluorescence staining of HeLa cells shows distinct signal patterns when counterstained with DAPI, while flow cytometry analysis of A549 cells confirms reliable detection with clear separation from isotype control, supporting quantitative single-cell applications.
This antibody supports researchers investigating stress response mechanisms, tumor microenvironment biology, and inflammatory signaling pathways where CIRBP function is increasingly recognized as therapeutically relevant.
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